Header list of 1k8m.pdb file
Complete list - 21 20 Bytes
HEADER TRANSFERASE 24-OCT-01 1K8M
TITLE SOLUTION STRUCTURE OF THE LIPOIC ACID-BEARING DOMAIN OF THE E2
TITLE 2 COMPONENT OF HUMAN, MITOCHONDRIAL BRANCHED-CHAIN ALPHA-KETOACID
TITLE 3 DEHYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E2 COMPONENT OF BRANCHED-CHAIN ALPHA-KETOACID
COMPND 3 DEHYDROGENASE;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: LIPOIC ACID-BEARING DOMAIN;
COMPND 6 SYNONYM: DIHYDROLIPOAMIDE BRANCHED CHAIN TRANSACYLASE;
COMPND 7 EC: 2.3.1.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS LIPOYL ACID BEARING, HUMAN BCKD, EXPERIMENTAL NMR DATA, AVERAGE
KEYWDS 2 STRUCTURE, TRANSFERASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR C.-F.CHANG,H.-T.CHOU,J.L.CHUANG,D.T.CHUANG,T.-H.HUANG
REVDAT 6 21-DEC-22 1K8M 1 SEQADV
REVDAT 5 23-FEB-22 1K8M 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1K8M 1 VERSN
REVDAT 3 01-APR-03 1K8M 1 JRNL
REVDAT 2 04-DEC-02 1K8M 1 REMARK
REVDAT 1 14-NOV-01 1K8M 0
JRNL AUTH C.-F.CHANG,H.-T.CHOU,J.L.CHUANG,D.T.CHUANG,T.-H.HUANG
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF THE LIPOIC ACID-BEARING
JRNL TITL 2 DOMAIN OF HUMAN MITOCHONDRIAL BRANCHED-CHAIN ALPHA-KETO ACID
JRNL TITL 3 DEHYDROGENASE COMPLEX
JRNL REF J.BIOL.CHEM. V. 277 15865 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11839747
JRNL DOI 10.1074/JBC.M110952200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, ARIA 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), NILGES ET. AL (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K8M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014696.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 310
REMARK 210 PH : 7.5; 7.5
REMARK 210 IONIC STRENGTH : 100MM NACL; 100MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM PROTEIN U-15N; 50MM
REMARK 210 PHOSPHATE BUFFER, PH7.5, 100MM
REMARK 210 NACL, 0.02% (W/V) NAN3; 2MM
REMARK 210 PROTEIN U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER, PH7.5, 100MM
REMARK 210 NACL, 0.02% (W/V) NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.0, AURELIA 2.0.6, ARIA
REMARK 210 1.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 88
REMARK 465 HIS A 89
REMARK 465 HIS A 90
REMARK 465 HIS A 91
REMARK 465 HIS A 92
REMARK 465 HIS A 93
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 C SER A 10 H ASP A 11 1.18
REMARK 500 O SER A 10 N ASP A 11 1.31
REMARK 500 O LEU A 86 HG2 GLU A 87 1.54
REMARK 500 H VAL A 32 O GLY A 56 1.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 1 N MET A 1 CA -0.645
REMARK 500 MET A 1 CA MET A 1 CB -0.757
REMARK 500 MET A 1 CB MET A 1 CG -0.683
REMARK 500 MET A 1 CG MET A 1 SD -0.998
REMARK 500 MET A 1 SD MET A 1 CE -1.268
REMARK 500 MET A 1 CA MET A 1 C -0.203
REMARK 500 MET A 1 C MET A 1 O -0.137
REMARK 500 GLY A 2 N GLY A 2 CA -0.196
REMARK 500 GLY A 2 C GLY A 2 O -0.202
REMARK 500 GLY A 2 C GLN A 3 N -0.170
REMARK 500 GLN A 3 CB GLN A 3 CG -0.425
REMARK 500 GLN A 3 CG GLN A 3 CD -0.500
REMARK 500 GLN A 3 CD GLN A 3 OE1 -0.875
REMARK 500 GLN A 3 CD GLN A 3 NE2 -0.734
REMARK 500 GLN A 6 CB GLN A 6 CG -0.284
REMARK 500 GLN A 6 CD GLN A 6 OE1 -0.418
REMARK 500 GLN A 6 CD GLN A 6 NE2 -0.265
REMARK 500 LYS A 8 CB LYS A 8 CG -0.400
REMARK 500 LYS A 8 CG LYS A 8 CD -0.238
REMARK 500 LYS A 8 CD LYS A 8 CE -0.174
REMARK 500 LYS A 8 CE LYS A 8 NZ -0.408
REMARK 500 SER A 10 CA SER A 10 CB -0.126
REMARK 500 SER A 10 CB SER A 10 OG -0.979
REMARK 500 SER A 10 C SER A 10 O -0.498
REMARK 500 SER A 10 C ASP A 11 N -0.336
REMARK 500 ASP A 11 CA ASP A 11 CB -0.138
REMARK 500 ASP A 11 CB ASP A 11 CG -0.784
REMARK 500 ASP A 11 CG ASP A 11 OD1 -0.477
REMARK 500 ASP A 11 CG ASP A 11 OD2 -0.784
REMARK 500 ILE A 12 CB ILE A 12 CG1 -0.318
REMARK 500 ILE A 12 CB ILE A 12 CG2 -0.471
REMARK 500 ILE A 12 C ILE A 12 O -0.115
REMARK 500 GLY A 13 C GLY A 13 O -0.145
REMARK 500 GLU A 14 CB GLU A 14 CG -0.784
REMARK 500 GLU A 14 CG GLU A 14 CD -0.505
REMARK 500 GLU A 14 CD GLU A 14 OE1 -0.519
REMARK 500 GLU A 14 CD GLU A 14 OE2 -0.639
REMARK 500 GLU A 14 C GLU A 14 O -0.269
REMARK 500 GLY A 15 N GLY A 15 CA -0.098
REMARK 500 GLY A 15 C GLY A 15 O -0.108
REMARK 500 ILE A 16 C ILE A 16 O -0.215
REMARK 500 ILE A 16 C ARG A 17 N -0.163
REMARK 500 ARG A 17 CB ARG A 17 CG -0.505
REMARK 500 ARG A 17 CG ARG A 17 CD -0.567
REMARK 500 ARG A 17 CD ARG A 17 NE -0.763
REMARK 500 ARG A 17 NE ARG A 17 CZ -0.373
REMARK 500 ARG A 17 CZ ARG A 17 NH1 -0.925
REMARK 500 ARG A 17 CZ ARG A 17 NH2 -0.738
REMARK 500 GLU A 18 CG GLU A 18 CD -0.273
REMARK 500 GLU A 18 CD GLU A 18 OE1 -0.473
REMARK 500
REMARK 500 THIS ENTRY HAS 192 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MET A 1 CB - CA - C ANGL. DEV. = 18.9 DEGREES
REMARK 500 MET A 1 N - CA - CB ANGL. DEV. = -26.1 DEGREES
REMARK 500 MET A 1 CA - CB - CG ANGL. DEV. = 45.7 DEGREES
REMARK 500 MET A 1 CB - CG - SD ANGL. DEV. = 54.0 DEGREES
REMARK 500 MET A 1 CG - SD - CE ANGL. DEV. = 36.1 DEGREES
REMARK 500 MET A 1 N - CA - C ANGL. DEV. = 22.2 DEGREES
REMARK 500 GLN A 3 CA - CB - CG ANGL. DEV. = 20.0 DEGREES
REMARK 500 GLN A 3 CB - CG - CD ANGL. DEV. = 33.0 DEGREES
REMARK 500 GLN A 3 OE1 - CD - NE2 ANGL. DEV. = -61.6 DEGREES
REMARK 500 GLN A 3 CG - CD - OE1 ANGL. DEV. = 22.1 DEGREES
REMARK 500 GLN A 3 CG - CD - NE2 ANGL. DEV. = 39.3 DEGREES
REMARK 500 GLN A 6 OE1 - CD - NE2 ANGL. DEV. = -15.5 DEGREES
REMARK 500 GLN A 6 CG - CD - NE2 ANGL. DEV. = 15.4 DEGREES
REMARK 500 LYS A 8 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 LYS A 8 CG - CD - CE ANGL. DEV. = 26.8 DEGREES
REMARK 500 SER A 10 CA - CB - OG ANGL. DEV. = 27.1 DEGREES
REMARK 500 SER A 10 CA - C - N ANGL. DEV. = 20.1 DEGREES
REMARK 500 SER A 10 O - C - N ANGL. DEV. = -25.0 DEGREES
REMARK 500 ASP A 11 C - N - CA ANGL. DEV. = 19.2 DEGREES
REMARK 500 ASP A 11 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 ASP A 11 CB - CG - OD1 ANGL. DEV. = 24.9 DEGREES
REMARK 500 ASP A 11 CB - CG - OD2 ANGL. DEV. = -34.4 DEGREES
REMARK 500 ILE A 12 CG1 - CB - CG2 ANGL. DEV. = -16.7 DEGREES
REMARK 500 ILE A 12 CA - CB - CG1 ANGL. DEV. = 16.9 DEGREES
REMARK 500 ILE A 12 CB - CG1 - CD1 ANGL. DEV. = 19.8 DEGREES
REMARK 500 GLU A 14 CA - CB - CG ANGL. DEV. = 31.2 DEGREES
REMARK 500 GLU A 14 CB - CG - CD ANGL. DEV. = 24.4 DEGREES
REMARK 500 GLU A 14 OE1 - CD - OE2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 GLU A 14 CG - CD - OE1 ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG A 17 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG A 17 CB - CG - CD ANGL. DEV. = 33.3 DEGREES
REMARK 500 ARG A 17 CG - CD - NE ANGL. DEV. = 43.9 DEGREES
REMARK 500 ARG A 17 CD - NE - CZ ANGL. DEV. = 45.0 DEGREES
REMARK 500 ARG A 17 NH1 - CZ - NH2 ANGL. DEV. = -88.0 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 40.9 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH2 ANGL. DEV. = 47.0 DEGREES
REMARK 500 GLU A 18 OE1 - CD - OE2 ANGL. DEV. = -21.9 DEGREES
REMARK 500 LYS A 22 CB - CG - CD ANGL. DEV. = 55.5 DEGREES
REMARK 500 LYS A 22 CG - CD - CE ANGL. DEV. = 52.8 DEGREES
REMARK 500 LYS A 22 CD - CE - NZ ANGL. DEV. = 46.4 DEGREES
REMARK 500 GLU A 23 CB - CG - CD ANGL. DEV. = 40.5 DEGREES
REMARK 500 GLU A 23 OE1 - CD - OE2 ANGL. DEV. = -15.5 DEGREES
REMARK 500 GLU A 23 CG - CD - OE2 ANGL. DEV. = 21.2 DEGREES
REMARK 500 TYR A 25 CB - CG - CD2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 TYR A 25 CD1 - CG - CD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 LYS A 27 CB - CG - CD ANGL. DEV. = 32.9 DEGREES
REMARK 500 LYS A 27 CG - CD - CE ANGL. DEV. = 36.3 DEGREES
REMARK 500 LYS A 27 CD - CE - NZ ANGL. DEV. = 27.2 DEGREES
REMARK 500 GLU A 28 OE1 - CD - OE2 ANGL. DEV. = -21.4 DEGREES
REMARK 500 GLU A 28 CG - CD - OE2 ANGL. DEV. = 15.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 122 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 11 -31.35 166.61
REMARK 500 ILE A 38 -74.85 -86.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5078 RELATED DB: BMRB
REMARK 900 5078 CONTAINS CHEMICAL SHIFT LISTS EXCLUDING FIRST MET RESIDUE
REMARK 900 RELATED ID: 1K8O RELATED DB: PDB
REMARK 900 1K8O CONTAINS 20 SRUCTURES OF THE SAME PROTEIN.
DBREF 1K8M A 2 85 UNP P11182 ODB2_HUMAN 62 145
SEQADV 1K8M MET A 1 UNP P11182 INITIATING METHIONINE
SEQADV 1K8M LEU A 86 UNP P11182 EXPRESSION TAG
SEQADV 1K8M GLU A 87 UNP P11182 EXPRESSION TAG
SEQADV 1K8M HIS A 88 UNP P11182 EXPRESSION TAG
SEQADV 1K8M HIS A 89 UNP P11182 EXPRESSION TAG
SEQADV 1K8M HIS A 90 UNP P11182 EXPRESSION TAG
SEQADV 1K8M HIS A 91 UNP P11182 EXPRESSION TAG
SEQADV 1K8M HIS A 92 UNP P11182 EXPRESSION TAG
SEQADV 1K8M HIS A 93 UNP P11182 EXPRESSION TAG
SEQRES 1 A 93 MET GLY GLN VAL VAL GLN PHE LYS LEU SER ASP ILE GLY
SEQRES 2 A 93 GLU GLY ILE ARG GLU VAL THR VAL LYS GLU TRP TYR VAL
SEQRES 3 A 93 LYS GLU GLY ASP THR VAL SER GLN PHE ASP SER ILE CYS
SEQRES 4 A 93 GLU VAL GLN SER ASP LYS ALA SER VAL THR ILE THR SER
SEQRES 5 A 93 ARG TYR ASP GLY VAL ILE LYS LYS LEU TYR TYR ASN LEU
SEQRES 6 A 93 ASP ASP ILE ALA TYR VAL GLY LYS PRO LEU VAL ASP ILE
SEQRES 7 A 93 GLU THR GLU ALA LEU LYS ASP LEU GLU HIS HIS HIS HIS
SEQRES 8 A 93 HIS HIS
SHEET 1 A 4 VAL A 5 LYS A 8 0
SHEET 2 A 4 PRO A 74 GLU A 79 -1 O ILE A 78 N VAL A 5
SHEET 3 A 4 GLY A 56 LEU A 61 -1 N VAL A 57 O GLU A 79
SHEET 4 A 4 THR A 31 VAL A 32 -1 N VAL A 32 O GLY A 56
SHEET 1 B 4 SER A 47 THR A 49 0
SHEET 2 B 4 CYS A 39 GLN A 42 -1 N VAL A 41 O VAL A 48
SHEET 3 B 4 VAL A 19 TRP A 24 -1 N GLU A 23 O GLU A 40
SHEET 4 B 4 ILE A 68 ALA A 69 -1 O ALA A 69 N VAL A 19
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 21 20 Bytes